GenomeNet

Database: PDB
Entry: 3Q96
LinkDB: 3Q96
Original site: 3Q96 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-JAN-11   3Q96              
TITLE     B-RAF KINASE DOMAIN IN COMPLEX WITH A TETRAHYDRONAPHTHALENE INHIBITOR 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 446-727;                                          
COMPND   5 SYNONYM: PROTO-ONCOGENE B-RAF, P94, V-RAF MURINE SARCOMA VIRAL       
COMPND   6 ONCOGENE HOMOLOG B1;                                                 
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRAF, BRAF1, RAFB1;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    DESIGN, OPTIMIZATION, POTENT, ORALLY BIOAVAILABLE,                    
KEYWDS   2 TETRAHYDRONAPHTHALENE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.D.SINTCHAK,K.AERTGEERTS,J.YANO                                      
REVDAT   3   08-NOV-17 3Q96    1       REMARK                                   
REVDAT   2   04-MAY-11 3Q96    1       JRNL                                     
REVDAT   1   23-MAR-11 3Q96    0                                                
JRNL        AUTH   A.E.GOULD,R.ADAMS,S.ADHIKARI,K.AERTGEERTS,R.AFROZE,          
JRNL        AUTH 2 C.BLACKBURN,E.F.CALDERWOOD,R.CHAU,J.CHOUITAR,M.O.DUFFEY,     
JRNL        AUTH 3 D.B.ENGLAND,C.FARRER,N.FORSYTH,K.GARCIA,J.GAULIN,            
JRNL        AUTH 4 P.D.GREENSPAN,R.GUO,S.J.HARRISON,S.C.HUANG,N.IARTCHOUK,      
JRNL        AUTH 5 D.JANOWICK,M.S.KIM,B.KULKARNI,S.P.LANGSTON,J.X.LIU,L.T.MA,   
JRNL        AUTH 6 S.MENON,H.MIZUTANI,E.PASKE,C.C.RENOU,M.REZAEI,R.S.ROWLAND,   
JRNL        AUTH 7 M.D.SINTCHAK,M.D.SMITH,S.G.STROUD,M.TREGAY,Y.TIAN,O.P.VEIBY, 
JRNL        AUTH 8 T.J.VOS,S.VYSKOCIL,J.WILLIAMS,T.XU,J.J.YANG,J.YANO,H.ZENG,   
JRNL        AUTH 9 D.M.ZHANG,Q.ZHANG,K.M.GALVIN                                 
JRNL        TITL   DESIGN AND OPTIMIZATION OF POTENT AND ORALLY BIOAVAILABLE    
JRNL        TITL 2 TETRAHYDRONAPHTHALENE RAF INHIBITORS.                        
JRNL        REF    J.MED.CHEM.                   V.  54  1836 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   21341678                                                     
JRNL        DOI    10.1021/JM101479Y                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 13851                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1381                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 831                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 90                           
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4075                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.95000                                              
REMARK   3    B22 (A**2) : 0.95000                                              
REMARK   3    B33 (A**2) : -1.91000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.536         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.376         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.366        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.897                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.835                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4250 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5760 ; 1.083 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   510 ; 5.023 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   177 ;36.607 ;23.785       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   745 ;18.515 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;17.593 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   637 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3153 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2558 ; 0.403 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4129 ; 0.747 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1692 ; 0.660 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1631 ; 1.185 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS; U VALUES: REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 3Q96 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063351.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14022                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 81.730                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.20600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.025% PEG 8000, 0.8M NP LITHIUM CL,    
REMARK 280  0.06M TRIS BASE, 0.04M TRIS CL, VAPOR DIFFUSION, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.63200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.01450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.01450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       41.31600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.01450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.01450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      123.94800            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.01450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.01450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       41.31600            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.01450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.01450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      123.94800            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.63200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   446                                                      
REMARK 465     SER A   447                                                      
REMARK 465     ASP A   448                                                      
REMARK 465     ALA A   598                                                      
REMARK 465     THR A   599                                                      
REMARK 465     VAL A   600                                                      
REMARK 465     LYS A   601                                                      
REMARK 465     SER A   602                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     TRP A   604                                                      
REMARK 465     SER A   605                                                      
REMARK 465     GLY A   606                                                      
REMARK 465     SER A   607                                                      
REMARK 465     HIS A   608                                                      
REMARK 465     GLN A   609                                                      
REMARK 465     PHE A   610                                                      
REMARK 465     GLU A   611                                                      
REMARK 465     GLN A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     SER A   614                                                      
REMARK 465     GLY A   615                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     ASP A   629                                                      
REMARK 465     LYS A   630                                                      
REMARK 465     LYS A   723                                                      
REMARK 465     ILE A   724                                                      
REMARK 465     HIS A   725                                                      
REMARK 465     ARG A   726                                                      
REMARK 465     SER A   727                                                      
REMARK 465     SER B   446                                                      
REMARK 465     SER B   447                                                      
REMARK 465     ASP B   448                                                      
REMARK 465     SER B   605                                                      
REMARK 465     GLY B   606                                                      
REMARK 465     SER B   607                                                      
REMARK 465     HIS B   608                                                      
REMARK 465     GLN B   609                                                      
REMARK 465     PHE B   610                                                      
REMARK 465     GLU B   611                                                      
REMARK 465     GLN B   612                                                      
REMARK 465     LEU B   613                                                      
REMARK 465     SER B   614                                                      
REMARK 465     LEU B   721                                                      
REMARK 465     PRO B   722                                                      
REMARK 465     LYS B   723                                                      
REMARK 465     ILE B   724                                                      
REMARK 465     HIS B   725                                                      
REMARK 465     ARG B   726                                                      
REMARK 465     SER B   727                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 462    NE   CZ   NH1  NH2                                  
REMARK 470     PHE A 468    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 522    CG   CD   CE   NZ                                   
REMARK 470     MET A 627    CG   SD   CE                                        
REMARK 470     LYS B 522    CG   CD   CE   NZ                                   
REMARK 470     ARG B 558    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 601    CG   CD   CE   NZ                                   
REMARK 470     MET B 627    CG   SD   CE                                        
REMARK 470     GLN B 628    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 629    CG   OD1  OD2                                       
REMARK 470     LYS B 630    CG   CD   CE   NZ                                   
REMARK 470     ARG B 691    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 709    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 463      -77.64    -81.94                                   
REMARK 500    PHE A 468      -77.80    -88.40                                   
REMARK 500    ARG A 509       80.53   -163.35                                   
REMARK 500    ILE A 543      -64.98   -106.61                                   
REMARK 500    GLU A 545       51.55     39.38                                   
REMARK 500    ARG A 575      -11.82     82.12                                   
REMARK 500    ASP A 576       51.21   -162.13                                   
REMARK 500    LEU A 588      -52.62   -141.23                                   
REMARK 500    ARG A 719      -71.79    -53.14                                   
REMARK 500    LEU A 721      -61.02   -154.00                                   
REMARK 500    PRO B 453      130.08    -36.77                                   
REMARK 500    ARG B 575      -12.97     73.28                                   
REMARK 500    ASP B 576       52.36   -155.40                                   
REMARK 500    LEU B 588       -5.47   -144.94                                   
REMARK 500    LEU B 597      -27.12     90.34                                   
REMARK 500    ARG B 626       -8.21    -57.76                                   
REMARK 500    SER B 679        1.41    -66.05                                   
REMARK 500    LEU B 716      -70.78    -79.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0NF A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0NF B 1                   
DBREF  3Q96 A  446   727  UNP    P15056   BRAF_HUMAN     446    727             
DBREF  3Q96 B  446   727  UNP    P15056   BRAF_HUMAN     446    727             
SEQRES   1 A  282  SER SER ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE THR          
SEQRES   2 A  282  VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR VAL          
SEQRES   3 A  282  TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS MET          
SEQRES   4 A  282  LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN ALA          
SEQRES   5 A  282  PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG HIS          
SEQRES   6 A  282  VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR LYS PRO          
SEQRES   7 A  282  GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER SER          
SEQRES   8 A  282  LEU TYR HIS HIS LEU HIS ILE ILE GLU THR LYS PHE GLU          
SEQRES   9 A  282  MET ILE LYS LEU ILE ASP ILE ALA ARG GLN THR ALA GLN          
SEQRES  10 A  282  GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS ARG          
SEQRES  11 A  282  ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP LEU          
SEQRES  12 A  282  THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR VAL LYS          
SEQRES  13 A  282  SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU SER          
SEQRES  14 A  282  GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG MET          
SEQRES  15 A  282  GLN ASP LYS ASN PRO TYR SER PHE GLN SER ASP VAL TYR          
SEQRES  16 A  282  ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY GLN          
SEQRES  17 A  282  LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE ILE          
SEQRES  18 A  282  PHE MET VAL GLY ARG GLY TYR LEU SER PRO ASP LEU SER          
SEQRES  19 A  282  LYS VAL ARG SER ASN CYS PRO LYS ALA MET LYS ARG LEU          
SEQRES  20 A  282  MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO          
SEQRES  21 A  282  LEU PHE PRO GLN ILE LEU ALA SER ILE GLU LEU LEU ALA          
SEQRES  22 A  282  ARG SER LEU PRO LYS ILE HIS ARG SER                          
SEQRES   1 B  282  SER SER ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE THR          
SEQRES   2 B  282  VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR VAL          
SEQRES   3 B  282  TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS MET          
SEQRES   4 B  282  LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN ALA          
SEQRES   5 B  282  PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG HIS          
SEQRES   6 B  282  VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR LYS PRO          
SEQRES   7 B  282  GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER SER          
SEQRES   8 B  282  LEU TYR HIS HIS LEU HIS ILE ILE GLU THR LYS PHE GLU          
SEQRES   9 B  282  MET ILE LYS LEU ILE ASP ILE ALA ARG GLN THR ALA GLN          
SEQRES  10 B  282  GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS ARG          
SEQRES  11 B  282  ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP LEU          
SEQRES  12 B  282  THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR VAL LYS          
SEQRES  13 B  282  SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU SER          
SEQRES  14 B  282  GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG MET          
SEQRES  15 B  282  GLN ASP LYS ASN PRO TYR SER PHE GLN SER ASP VAL TYR          
SEQRES  16 B  282  ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY GLN          
SEQRES  17 B  282  LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE ILE          
SEQRES  18 B  282  PHE MET VAL GLY ARG GLY TYR LEU SER PRO ASP LEU SER          
SEQRES  19 B  282  LYS VAL ARG SER ASN CYS PRO LYS ALA MET LYS ARG LEU          
SEQRES  20 B  282  MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO          
SEQRES  21 B  282  LEU PHE PRO GLN ILE LEU ALA SER ILE GLU LEU LEU ALA          
SEQRES  22 B  282  ARG SER LEU PRO LYS ILE HIS ARG SER                          
HET    0NF  A   1      39                                                       
HET    0NF  B   1      39                                                       
HETNAM     0NF (2S)-N-[3-(2-AMINOPROPAN-2-YL)-5-(TRIFLUOROMETHYL)               
HETNAM   2 0NF  PHENYL]-7-[(7-OXO-5,6,7,8-TETRAHYDRO-1,8-NAPHTHYRIDIN-          
HETNAM   3 0NF  4-YL)OXY]-1,2,3,4-TETRAHYDRONAPHTHALENE-2-CARBOXAMIDE           
FORMUL   3  0NF    2(C29 H29 F3 N4 O3)                                          
HELIX    1   1 THR A  491  ARG A  506  1                                  16    
HELIX    2   2 LEU A  537  ILE A  543  1                                   7    
HELIX    3   3 GLU A  549  LYS A  570  1                                  22    
HELIX    4   4 LYS A  578  ASN A  580  5                                   3    
HELIX    5   5 ALA A  621  MET A  627  1                                   7    
HELIX    6   6 SER A  634  GLY A  652  1                                  19    
HELIX    7   7 ASN A  661  GLY A  672  1                                  12    
HELIX    8   8 ASP A  677  VAL A  681  5                                   5    
HELIX    9   9 PRO A  686  LEU A  697  1                                  12    
HELIX   10  10 LYS A  700  ARG A  704  5                                   5    
HELIX   11  11 LEU A  706  SER A  720  1                                  15    
HELIX   12  12 THR B  491  ARG B  506  1                                  16    
HELIX   13  13 SER B  536  ILE B  543  1                                   8    
HELIX   14  14 GLU B  549  LYS B  570  1                                  22    
HELIX   15  15 GLU B  586  LEU B  588  5                                   3    
HELIX   16  16 ALA B  621  ARG B  626  1                                   6    
HELIX   17  17 SER B  634  GLY B  652  1                                  19    
HELIX   18  18 ASN B  661  ARG B  671  1                                  11    
HELIX   19  19 ASP B  677  VAL B  681  5                                   5    
HELIX   20  20 PRO B  686  LEU B  697  1                                  12    
HELIX   21  21 LYS B  700  ARG B  704  5                                   5    
HELIX   22  22 LEU B  706  ALA B  718  1                                  13    
SHEET    1   A 5 THR A 458  SER A 465  0                                        
SHEET    2   A 5 THR A 470  LYS A 475 -1  O  VAL A 471   N  GLY A 464           
SHEET    3   A 5 ASP A 479  MET A 484 -1  O  MET A 484   N  THR A 470           
SHEET    4   A 5 ALA A 526  GLN A 530 -1  O  THR A 529   N  ALA A 481           
SHEET    5   A 5 PHE A 516  SER A 520 -1  N  GLY A 518   O  VAL A 528           
SHEET    1   B 3 GLY A 534  SER A 536  0                                        
SHEET    2   B 3 ILE A 582  HIS A 585 -1  O  LEU A 584   N  SER A 535           
SHEET    3   B 3 THR A 589  ILE A 592 -1  O  THR A 589   N  HIS A 585           
SHEET    1   C 5 THR B 458  GLY B 466  0                                        
SHEET    2   C 5 GLY B 469  LYS B 475 -1  O  VAL B 471   N  GLY B 464           
SHEET    3   C 5 ASP B 479  MET B 484 -1  O  VAL B 482   N  TYR B 472           
SHEET    4   C 5 ALA B 526  GLN B 530 -1  O  ILE B 527   N  LYS B 483           
SHEET    5   C 5 PHE B 516  SER B 520 -1  N  GLY B 518   O  VAL B 528           
SHEET    1   D 2 ILE B 582  HIS B 585  0                                        
SHEET    2   D 2 THR B 589  ILE B 592 -1  O  LYS B 591   N  PHE B 583           
CISPEP   1 LYS A  522    PRO A  523          0        11.57                     
CISPEP   2 LYS B  522    PRO B  523          0         5.01                     
SITE     1 AC1 15 ALA A 481  LYS A 483  GLU A 501  LEU A 505                    
SITE     2 AC1 15 LEU A 514  ILE A 527  THR A 529  GLN A 530                    
SITE     3 AC1 15 TRP A 531  CYS A 532  LEU A 567  HIS A 574                    
SITE     4 AC1 15 GLY A 593  ASP A 594  PHE A 595                               
SITE     1 AC2 15 VAL B 471  ALA B 481  LYS B 483  GLU B 501                    
SITE     2 AC2 15 VAL B 504  LEU B 514  GLN B 530  TRP B 531                    
SITE     3 AC2 15 CYS B 532  HIS B 574  PHE B 583  GLY B 593                    
SITE     4 AC2 15 ASP B 594  PHE B 595  ALA B 598                               
CRYST1   94.029   94.029  165.264  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010635  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006051        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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